Linked Life Data

11142349

Source:http://linkedlifedata.com/resource/pubmed/id/11142349

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-1-4
pubmed:abstractText
An extracellular proteinase of Acanthamoeba castellanii was purified and its biochemical and pathological properties were characterized. The molecular mass of the purified enzyme was approximately 42 kDa as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Sephacryl S-200 HR gel-filtration chromatography. Therefore, its structure seemed to be monomeric with a single polypeptide. Its activity was inhibited by the serine proteinase inhibitors diisopropyl fluorophosphate and phenylmethanesulfonyl fluoride. Its activity was optimum at 30 to 50 degrees C with a maximum at 50 degrees C; optimal pH was 8.0. As much as 70% of the enzyme activity was maintained at 50 degrees C for at least 12 h but was rapidly inactivated thereafter. The purified enzyme degraded collagen and rabbit corneal extract. Furthermore, it exhibited strong cytopathic effects on human corneal epithelial cells and fibroblast cells. These suggest the possible role of this enzyme in the pathogenesis of Acanthamoeba.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1521-6543
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
209-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Purification and characterization of an extracellular serine proteinase from Acanthamoeba castellanii.
pubmed:affiliation
Department of Biology, College of Natural Science, Chung-Ang University, Seoul, Korea.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't